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Gewählte Publikation:

Coman, V., Harreither, W., Ludwig, R., Haltrich, D., and Gorton, L..
(2007): Investigation of Electron Transfer Between Cellobiose Dehydrogenase From Myriococcum Thermophilum and Gold Electrodes
CHEM ANAL-WARSAW, 52, 954-960; ISSN 0009-2223

Cellobiose dehydrogenase (CDH) is a monomeric protein consisting of two subdomains: a larger flavin-associated domain (DHcdh) and a smaller heme-binding domain (CYTcdh), connected via a protease cleavable linker region. In this study, the inter-domain electron transfer, using the CDH from the ascomycete fungus Myriococcum thermophilum and thiol (SAM) modified gold electrodes, was investigated with cyclic voltammetry and UV-VIS spectroelectrochemistry. The effect of the SAM and pH on the formal potential of the heme domain of CDH and on the current generated by the electrocatalytic oxidation of cellobiose and lactose was evaluated with voltammetric techniques. The oxidation-reduction midpoint potentials of the DHcdh, CYTcdh, and whole CDH unit were estimated at different pH values using a long-optical-pathway thin capillary-type spectroelectrochemical cell.
Autor/innen der BOKU Wien:
Haltrich Dietmar
Harreither Wolfgang
Ludwig Roland
BOKU Gendermonitor:

Find related publications in this database (Keywords)
cellobiose dehydrogenase
Myriococcum thermophilum
thiol modified gold electrode
direct electron transfer

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